Analytical Data
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Gene name
TRIM52
- Application
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Alternative Names
TRIM52; RNF102; E3 ubiquitin-Protein ligase TRIM52; EC 2.3.2.27; RING finger Protein 102; Tripartite motif-containing Protein 52
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96A61
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Expression Region
1-297 aa
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AA Sequence
MAGYATTPSP MQTLQEEAVC AICLDYFKDP VSISCGHNFC RGCVTQLWSK EDEEDQNEEE DEWEEEEDEE AVGAMDGWDG SIREVLYRGN ADEELFQDQD DDELWLGDSG ITNWDNVDYM WDEEEEEEEE DQDYYLGGLR PDLRIDVYRE EEILEAYDED EDEELYPDIH PPPSLPLPGQ FTCPQCRKSF TRRSFRPNLQ LANMVQIIRQ MCPTPYRGNR SNDQGMCFKH QEALKLFCEV DKEAICVVCR ESRSHKQHSV LPLEEVVQEY QEIKLETTLV GILQIEQESI HSKAYNQ
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Molecular Weight
34.6 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The TRIM52 protein, a member of the tripartite motif (TRIM) family, has garnered attention for its potential roles in cellular processes, including immune response, cell proliferation, and oncogenesis. Research into TRIM proteins has shown that they are involved in various biological functions such as autophagy, viral defense, and modulation of signaling pathways, making them crucial for understanding cellular homeostasis and pathophysiological conditions. TRIM52, in particular, is thought to play a role in the regulation of cell growth and differentiation, with implications in cancer biology. Preliminary studies suggest that TRIM52 may interact with key cellular pathways and proteins that influence tumorigenesis, presenting an opportunity for deeper exploration into its molecular mechanisms. Additionally, investigations into the post-translational modifications and interacting partners of TRIM52 could provide insights into its functional diversity and regulatory roles within the cell. Understanding TRIM52’s actions may lay the groundwork for novel therapeutic strategies targeting TRIM proteins in cancer and other diseases, highlighting the importance of further research in this area to elucidate the precise functions and implications of TRIM52 in health and disease.
